(data stored in ACNUC7421 zone)

SWISSPROT: Q13IJ3_PARXL

ID   Q13IJ3_PARXL            Unreviewed;       469 AA.
AC   Q13IJ3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   SubName: Full=Putative cytochrome c, class I {ECO:0000313|EMBL:ABE36096.1};
GN   ORFNames=Bxe_C0171 {ECO:0000313|EMBL:ABE36096.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36096.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36096.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36096.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- PTM: Binds 3 heme groups per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000018-50}.
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DR   EMBL; CP000272; ABE36096.1; -; Genomic_DNA.
DR   RefSeq; WP_011493356.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0171; -.
DR   EnsemblBacteria; ABE36096; ABE36096; Bxe_C0171.
DR   GeneID; 4009719; -.
DR   KEGG; bxb:DR64_8258; -.
DR   KEGG; bxe:Bxe_C0171; -.
DR   PATRIC; fig|266265.5.peg.7953; -.
DR   eggNOG; ENOG4105CE2; Bacteria.
DR   eggNOG; COG1529; LUCA.
DR   HOGENOM; HOG000178965; -.
DR   OMA; AYGSMVE; -.
DR   OrthoDB; 1297285at2; -.
DR   BioCyc; BXEN266265:BXE_RS37590-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.760.10; -; 3.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR   Pfam; PF13442; Cytochrome_CBB3; 2.
DR   PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR   SUPFAM; SSF46626; SSF46626; 3.
DR   PROSITE; PS51007; CYTC; 3.
PE   4: Predicted;
DR   PRODOM; Q13IJ3.
DR   SWISS-2DPAGE; Q13IJ3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Heme {ECO:0000256|PIRSR:PIRSR000018-50, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Iron {ECO:0000256|PIRSR:PIRSR000018-51, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000018-51, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    469       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004182222.
FT   DOMAIN       72    176       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      219    332       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      358    448       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   METAL        90     90       Iron (heme 1 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   METAL       238    238       Iron (heme 2 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   METAL       375    375       Iron (heme 3 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   BINDING      86     86       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING      89     89       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     234    234       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     237    237       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     371    371       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     374    374       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
SQ   SEQUENCE   469 AA;  50048 MW;  6BB6906908A931B5 CRC64;
     MKPRPLMAGA TARRHAALCA CMAALAVAVA GVATREARSE EARAPAGPAT VLPSASARPA
     LPQPASPQPD AVMLARGEYI AKASDCAGCH TAPQGGAPYA GGNGLGSPFG TIMSTNITPD
     PHYGIGQYTY DDFARVLRKG VARGGKRLYP AMPYNAFAKI DDADLHALYA YMMHGVAPVA
     KPNRKSDVSF PFNQRWGLWF WQLAFVPREP YQPHADRDAQ WNRGAYLVQS VGHCGSCHTP
     RGIAYQERGT DESSSTFLTG GVNDHWFAPD LTGDAGSGLG RWRASEIAAF LKTGHGGGNI
     AYGSMVEQIE DSSQYLTDDD LLAIGRYLKS LPPRNPSATY APHDDVARKP LNGSRVPEAL
     SVGYNVYRSF CAQCHGGDGR GVPNVFPALA GNSSVLAEDT TSLIRLLVEG GNSPSTLTGP
     PRQQMPRFAD TLADVQIGQV LTYIRSAWGN NAQPITANDV SSLRQKLHK
//

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